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Specific antibodies to the N-termini of the interpeptide bridges of peptidoglycan

Specific antibodies to the N-termini of the interpeptide bridges of peptidoglycan 203 118 118 2 2 Peter H. Seidl Karl H. Schleifer Lehrstuhl für Mikrobiologie der Technischen Universität München Arcisstr. 21 D-8000 München 2 Federal Republic of Germany Abstract The synthetic peptides Gly 5 -ε-Ahx and l -Ala 3 -ε-Ahx, with structural similarity to the interpeptide bridge peptides of staphylococci or micrococci, respectively, were covalently linked to human serum albumin via their carboxylgroups. Antisera to these synthetic peptidyl-protein antigens contained fairly high amounts of antibodies with specificity to the N-terminal parts of the peptide chains attached to the carrier proteins. Antisera to (Gly 5 -ε-Ahx) 20 -albumin gave, without exception, strong precipitin reactions in latex-agglutination with staphylococcal peptidoglycans. The antisera completely failed, however, in any reaction with peptidoglycans of micrococci or other bacteria which did not have these oligo-glycine peptides typical for staphylococci. On the contrary, antisera to ( l -Ala 3 -ε-Ahx) 22 -albumin strongly precipitated micrococcal peptidoglycans with oligo- l -alanine interpeptide bridges (e.g. Micrococcus varians, Micrococcus reseus ), but showed no significant reaction with peptidoglycans of staphylococci or other bacteria lacking oligo- l -alanine interpeptide bridges. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Microbiology Springer Journals

Specific antibodies to the N-termini of the interpeptide bridges of peptidoglycan

Archives of Microbiology , Volume 118 (2) – Aug 1, 1978

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References (25)

Publisher
Springer Journals
Copyright
Copyright © 1978 by Springer-Verlag
Subject
Life Sciences; Biotechnology; Biochemistry, general; Cell Biology; Ecology; Microbial Ecology; Microbiology
ISSN
0302-8933
eISSN
1432-072X
DOI
10.1007/BF00415728
Publisher site
See Article on Publisher Site

Abstract

203 118 118 2 2 Peter H. Seidl Karl H. Schleifer Lehrstuhl für Mikrobiologie der Technischen Universität München Arcisstr. 21 D-8000 München 2 Federal Republic of Germany Abstract The synthetic peptides Gly 5 -ε-Ahx and l -Ala 3 -ε-Ahx, with structural similarity to the interpeptide bridge peptides of staphylococci or micrococci, respectively, were covalently linked to human serum albumin via their carboxylgroups. Antisera to these synthetic peptidyl-protein antigens contained fairly high amounts of antibodies with specificity to the N-terminal parts of the peptide chains attached to the carrier proteins. Antisera to (Gly 5 -ε-Ahx) 20 -albumin gave, without exception, strong precipitin reactions in latex-agglutination with staphylococcal peptidoglycans. The antisera completely failed, however, in any reaction with peptidoglycans of micrococci or other bacteria which did not have these oligo-glycine peptides typical for staphylococci. On the contrary, antisera to ( l -Ala 3 -ε-Ahx) 22 -albumin strongly precipitated micrococcal peptidoglycans with oligo- l -alanine interpeptide bridges (e.g. Micrococcus varians, Micrococcus reseus ), but showed no significant reaction with peptidoglycans of staphylococci or other bacteria lacking oligo- l -alanine interpeptide bridges.

Journal

Archives of MicrobiologySpringer Journals

Published: Aug 1, 1978

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